Isolation of the Fourth Enzyme (Isomerase) of Histidine Biosynthesis from Salmonella typhimurium
作者： Michael N. Margolies , Robert F. Goldberger
DOI: 10.1016/S0021-9258(18)96459-8
关键词: Histidine 、 Ammonium sulfate 、 Chromatography 、 Biochemistry 、 Isomerase 、 Size-exclusion chromatography 、 Sephadex 、 Enzyme 、 Protamine sulfate 、 Ion chromatography 、 Chemistry
摘要: Abstract A method is presented for the purification of isomerase catalyzing fourth step histidine biosynthesis in Salmonella typhimurium. The enzyme was isolated from extracts auxotrophs which (when derepressed) produced 25 to 30 times wild type levels enzyme. procedure involved fractionation with protamine sulfate and ammonium sulfate, gel filtration on Sephadex G-100, ion exchange chromatography diethylaminoethyl Sephadex, continuous flow high voltage electrophoresis. final product homogeneous respect size, a weight average molecular 29,000, but composed three enzymically active forms (in ratio 90:9:1) may be distinguished by their differing electrophoretic mobilities alkaline polyacrylamide gels.
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